1p53
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(New page: 200px<br /> <applet load="1p53" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p53, resolution 3.06Å" /> '''The Crystal Structu...)
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Revision as of 16:33, 12 November 2007
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The Crystal Structure of ICAM-1 D3-D5 fragment
Contents |
Overview
We have determined the 3.0 A crystal structure of the three C-terminal, domains 3-5 (D3-D5) of ICAM-1. Combined with the previously known, N-terminal two-domain structure (D1D2), a model of an entire ICAM-1, extracellular fragment has been constructed. This model should represent a, general architecture of other ICAM family members, particularly ICAM-3 and, ICAM-5. The observed intimate dimerization interaction at D4 and a stiff, D4-D5 stem-like architecture provide a good structural explanation for the, existence of preformed ICAM-1 cis dimers on the cell membrane. Together, with another dimerization interface at D1, a band-like one-dimensional, linear cluster of ICAM-1 on an antigen-presenting cell (APC) surface can, be envisioned, which might explain the formation of an immunological, synapse between an activated T cell and APC which is critical for T cell, receptor signaling.
Disease
Known disease associated with this structure: Malaria, cerebral, susceptibility to OMIM:[147840]
About this Structure
1P53 is a Single protein structure of sequence from Homo sapiens with NAG and NDG as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis for dimerization of ICAM-1 on the cell surface., Yang Y, Jun CD, Liu JH, Zhang R, Joachimiak A, Springer TA, Wang JH, Mol Cell. 2004 Apr 23;14(2):269-76. PMID:15099525
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Categories: Homo sapiens | Single protein | Jochimiak, A. | Jun, C.D. | Liu, J.H. | Springer, T.A. | Wang, J.H. | Yang, Y. | Zhang, R. | NAG | NDG | Beta-sheet | Dimer | Igsf domain